ID   PNG1_GIBMO              Reviewed;         450 AA.
AC   Q8J2R3;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Protein PNG1;
GN   Name=PNG1;
OS   Gibberella moniliformis (Maize ear and stalk rot fungus) (Fusarium
OS   verticillioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=117187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M3125 / FGSC 7600;
RX   PubMed=16536629; DOI=10.1021/jf0527706;
RA   Proctor R.H., Plattner R.D., Desjardins A.E., Busman M., Butchko R.A.;
RT   "Fumonisin production in the maize pathogen Fusarium verticillioides:
RT   genetic basis of naturally occurring chemical variation.";
RL   J. Agric. Food Chem. 54:2424-2430(2006).
CC   -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Although strongly related to the peptide:N-glycanase enzyme,
CC       it lacks the conserved active site Cys in position 243, which is
CC       replaced by a Val residue suggesting that it has no activity.
CC       {ECO:0000305}.
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DR   EMBL; AF155773; AAN74810.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J2R3; -.
DR   SMR; Q8J2R3; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   Pfam; PF03835; Rad4; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Zinc.
FT   CHAIN           1..450
FT                   /note="Protein PNG1"
FT                   /id="PRO_0000248990"
FT   REGION          32..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  50986 MW;  DE9A52868DE947E2 CRC64;
     MAGQRTPAGE YGEEWARDLR VQFEGLLRDK RMNDLRASSR QGSPSSGEQS PRMRGSPFPS
     DSRPSTSQGP GLPSYSALRH LPKIPTPPAA GDRDSQKFRN LLISLSLTPT KYENPGLLDE
     ALQTIPLDRI YGEAEEETQV LQAQAESMGD GRRPEWGYQD CVIRALLRWF KRSFFSWVNN
     PPCPVCLSPT IARGMTAPSP EESACGALRV ELYQCSAQHC GAFERFPRYG DVWRLLQTRR
     GRVGEWANCF SMLCRAVGGR VRWVWNAEDH VWTEVYSDHQ KRWVHVDACE EAWDNPRLLA
     EGWGKKMSYC IAFSIDGATD VTRRYVRKNQ HAAERNRCPE EVLLYVMQEI KNMRRSNMNK
     DERFRLEKED SREDNELRGY VVASIAQAVT DLVPGSPGGS NHTGASGSDT KLPAEQPGRQ
     TGSTEWLTAQ QQQSGRYQQP RDPSHRRPLP